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1KWM

Human procarboxypeptidase B: Three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031410cellular_componentcytoplasmic vesicle
A0046872molecular_functionmetal ion binding
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031410cellular_componentcytoplasmic vesicle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AHIS69
AGLU72
AASN144
AHIS196
AHOH1352

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 400
ChainResidue
BHOH761
BHIS69
BGLU72
BASN144
BHIS196

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 900
ChainResidue
ALEU78
AHIS133
AGLY135
ASER136
ATYR165
APRO168
AARG276
AHOH967
AHOH990
AHOH1121
AHOH1174
AHOH1185
AHOH1197

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIfMdcGfHArEwISPafcqwF
ChainResidueDetails
APRO60-PHE82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQMMiYPY
ChainResidueDetails
AHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AGLU270
BGLU270

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12162965
ChainResidueDetails
AHIS69
AGLU72
AHIS196
BHIS69
BGLU72
BHIS196

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248
BARG127
BASN144
BSER197
BTYR248

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG127
AGLU270

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG127
BGLU270

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG71
BGLU270
BARG127

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PDB entries from 2024-08-14

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